Mouse Anti-F2RL1 Recombinant Antibody (CBXF-0161) (CBMAB-F0259-CQ)

Mouse

Human

CBXF-0161

IgG2a

ELISA, IF, WB

Human

IgG2a

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Liquid

PBS, pH 7.2

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

F2R Like Trypsin Receptor 1

This gene encodes a member of the G-protein coupled receptor 1 family of proteins. The encoded cell surface receptor is activated through proteolytic cleavage of its extracellular amino terminus, resulting in a new amino terminus that acts as a tethered ligand that binds to an extracellular loop domain. Activation of the receptor has been shown to stimulate vascular smooth muscle relaxation, dilate blood vessels, increase blood flow, and lower blood pressure. This protein is also important in the inflammatory response, as well as innate and adaptive immunity.

F2R Like Trypsin Receptor 1; Coagulation Factor II (Thrombin) Receptor-Like 1; G-Protein Coupled Receptor 11; Thrombin Receptor-Like 1; GPR11; PAR2;

Receptor for trypsin and trypsin-like enzymes coupled to G proteins (PubMed:28445455).

Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho (PubMed:28445455).

Can also be transactivated by cleaved F2R/PAR1. Involved in modulation of inflammatory responses and regulation of innate and adaptive immunity, and acts as a sensor for proteolytic enzymes generated during infection. Generally is promoting inflammation. Can signal synergistically with TLR4 and probably TLR2 in inflammatory responses and modulates TLR3 signaling. Has a protective role in establishing the endothelial barrier; the activity involves coagulation factor X. Regulates endothelial cell barrier integrity during neutrophil extravasation, probably following proteolytic cleavage by PRTN3 (PubMed:23202369).

Proposed to have a bronchoprotective role in airway epithelium, but also shown to compromise the airway epithelial barrier by interrupting E-cadherin adhesion (PubMed:10086357).

Involved in the regulation of vascular tone; activation results in hypotension presumably mediated by vasodilation. Associates with a subset of G proteins alpha subunits such as GNAQ, GNA11, GNA14, GNA12 and GNA13, but probably not with G(o) alpha, G(i) subunit alpha-1 and G(i) subunit alpha-2. However, according to PubMed:21627585 can signal through G(i) subunit alpha. Believed to be a class B receptor which internalizes as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptor, for extended periods of time. Mediates inhibition of TNF-alpha stimulated JNK phosphorylation via coupling to GNAQ and GNA11; the function involves dissociation of RIPK1 and TRADD from TNFR1. Mediates phosphorylation of nuclear factor NF-kappa-B RELA subunit at 'Ser-536'; the function involves IKBKB and is predominantly independent of G proteins. Involved in cellular migration. Involved in cytoskeletal rearrangement and chemotaxis through beta-arrestin-promoted scaffolds; the function is independent of GNAQ and GNA11 and involves promotion of cofilin dephosphorylation and actin filament severing. Induces redistribution of COPS5 from the plasma membrane to the cytosol and activation of the JNK cascade is mediated by COPS5. Involved in the recruitment of leukocytes to the sites of inflammation and is the major PAR receptor capable of modulating eosinophil function such as proinflammatory cytokine secretion, superoxide production and degranulation. During inflammation promotes dendritic cell maturation, trafficking to the lymph nodes and subsequent T-cell activation. Involved in antimicrobial response of innate immune cells; activation enhances phagocytosis of Gram-positive and killing of Gram-negative bacteria. Acts synergistically with interferon-gamma in enhancing antiviral responses. Implicated in a number of acute and chronic inflammatory diseases such as of the joints, lungs, brain, gastrointestinal tract, periodontium, skin, and vascular systems, and in autoimmune disorders.

Bblood coagulation Source: InterPro
Cell-cell junction maintenance Source: UniProtKB
Defense response to virus Source: UniProtKB
Establishment of endothelial barrier Source: UniProtKB
G protein-coupled receptor signaling pathway Source: UniProtKB
Inflammatory response Source: UniProtKB-KW
Innate immune response Source: UniProtKB-KW
Leukocyte migration Source: UniProtKB
Leukocyte proliferation Source: UniProtKB
Mature conventional dendritic cell differentiation Source: UniProtKB
Negative regulation of chemokine production Source: UniProtKB
Negative regulation of JNK cascade Source: UniProtKB
Negative regulation of toll-like receptor 3 signaling pathway Source: UniProtKB
Negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Neutrophil activation Source: UniProtKB
Positive regulation of actin filament depolymerization Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Positive regulation of chemokine production Source: UniProtKB
Positive regulation of chemotaxis Source: UniProtKB
Positive regulation of cytokine production involved in immune response Source: UniProtKB
Positive regulation of cytosolic calcium ion concentration Source: UniProtKB
Positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling Pathway Source: GO_Central
Positive regulation of eosinophil degranulation Source: UniProtKB
Positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
Positive regulation of glomerular filtration Source: UniProtKB
Positive regulation of GTPase activity Source: UniProtKB
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of interferon-gamma production Source: UniProtKB
Positive regulation of interleukin-10 production Source: UniProtKB
Positive regulation of interleukin-1 beta production Source: UniProtKB
Positive regulation of interleukin-6 production Source: UniProtKB
Positive regulation of interleukin-8 production Source: UniProtKB
Positive regulation of JNK cascade Source: UniProtKB
Positive regulation of leukocyte chemotaxis Source: BHF-UCL
Positive regulation of neutrophil mediated killing of gram-negative bacterium Source: UniProtKB
Positive regulation of phagocytosis, engulfment Source: UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
Positive regulation of positive chemotaxis Source: BHF-UCL
Positive regulation of pseudopodium assembly Source: UniProtKB
Positive regulation of renin secretion into blood stream Source: UniProtKB
Positive regulation of Rho protein signal transduction Source: UniProtKB
Positive regulation of superoxide anion generation Source: UniProtKB
Positive regulation of toll-like receptor 2 signaling pathway Source: UniProtKB
Positive regulation of toll-like receptor 3 signaling pathway Source: UniProtKB
Positive regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Regulation of blood coagulation Source: BHF-UCL
Regulation of chemokine (C-X-C motif) ligand 2 production Source: UniProtKB
Regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Regulation of JNK cascade Source: UniProtKB
T cell activation involved in immune response Source: UniProtKB
Vasodilation Source: UniProtKB

Cell membrane

Extracellular: 37-71
Helical: 72-101
Cytoplasmic: 102-108
Helical: 109-137
Extracellular: 138-149
Helical: 150-177
Cytoplasmic: 178-183
Helical: 184-211
Extracellular: 212-235
Helical: 236-269
Cytoplasmic: 270-277
Helical: 278-317
Extracellular: 318-323
Helical: 324-347
Cytoplasmic: 348-397

A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand (PubMed:10831593, PubMed:19864598, PubMed:9020112, PubMed:10805786, PubMed:16478888). Activating serine proteases include trypsin, mast cell tryptase, coagulation factors VII and Xa, myeloblastin/PRTN3 and membrane-type serine protease 1/ST14 (PubMed:10831593, PubMed:19864598, PubMed:9020112, PubMed:10805786, PubMed:16478888, PubMed:23202369). Subsequent cleavage by serine proteases, including neutrophil elastase and cathepsin G, leads to receptor deactivation (PubMed:12594060). At least in part, implicated proteases are also shown to activate the receptor; the glycosylation status of the receptor is thought to contribute to the difference (PubMed:12171601). In addition to conventional trypsin-like proteases activated by other proteases and glycosidases derived from bacteria, fungi and insects (PubMed:11447194, PubMed:11441110, PubMed:17404307, PubMed:18474671, PubMed:19864598). Activated by serine protease allergens such as dust mite Der p3 and Der p9 and mold Pen c13 (PubMed:11441110, PubMed:17404307). Activated by P.gingivalis arginine-specific (trypsin-like) cysteine proteinases called gingipains (PubMed:11447194). Activated by S.griseus exogenous chitinase (PubMed:18474671). Activated by A.alternata aspartate protease; the cleavage generates non-conventional processed forms (PubMed:19864598).
N-glycosylated and sialylated.
Multiple phosphorylated on serine and threonine residues in the cytoplasmic region upon receptor activation; required for receptor desensitization and recruitment of beta-arrestin.
Monoubiquitinated by CBL at the plasma membrane and in early endosomes; not required for receptor endocytosis but for translocation to late endosomes or lysosomes. Deubiquitination involves STAMBP and USP8; required for lysosomal trafficking and receptor degradation.